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Q15149 (PLEC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plectin

Short name=PCN
Short name=PLTN
Alternative name(s):
Hemidesmosomal protein 1
Short name=HD1
Plectin-1
Gene names
Name:PLEC
Synonyms:PLEC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4684 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity. Ref.6 Ref.18

Subunit structure

Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via CH 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A. Interacts with ANK3. Ref.6 Ref.13 Ref.19 Ref.23

Subcellular location

Cytoplasmcytoskeleton. Cell junctionhemidesmosome Ref.6.

Tissue specificity

Widely expressed with highest levels in muscle, heart, placenta and spinal cord.

Domain

The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4.

Post-translational modification

Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis By similarity. Ref.5

Involvement in disease

Epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]: Autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Epidermolysis bullosa simplex, with muscular dystrophy (MD-EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the association of blister formation at the level of the hemidesmosome with late-onset muscular dystrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.20 Ref.27 Ref.28

Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.29

Limb-girdle muscular dystrophy 2Q (LGMD2Q) [MIM:613723]: A form of limb-girdle muscular dystrophy characterized by early childhood onset of proximal muscle weakness. Limb-girdle muscular dystrophies are characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. A 9 bp deletion containing the initiation codon in exon 1f of PLEC have been found in limb-girdle muscular dystrophy patients. The mutation results in deficient expression of isoform 9 and disorganization of the myofibers, without any effect on the skin. Ref.2 Ref.18

Sequence similarities

Belongs to the plakin or cytolinker family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 33 plectin repeats.

Contains 4 spectrin repeats.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epidermolysis bullosa
Limb-girdle muscular dystrophy
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

hemidesmosome assembly

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcostamere

Traceable author statement Ref.23. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

focal adhesion

Inferred from direct assay. Source: HPA

hemidesmosome

Inferred from direct assay Ref.6. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

plasma membrane

Non-traceable author statement Ref.1. Source: ProtInc

sarcolemma

Inferred from direct assay Ref.18. Source: UniProtKB

sarcoplasm

Inferred from sequence or structural similarity Ref.23. Source: BHF-UCL

   Molecular_functionankyrin binding

Inferred from physical interaction Ref.23. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.13Ref.19. Source: UniProtKB

structural constituent of muscle

Inferred from mutant phenotype Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15149-1)

Also known as: Plectin-6;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15149-2)

Also known as: Plectin-1; 1c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
Note: Contains a phosphoserine at position 42.
Isoform 3 (identifier: Q15149-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
     409-412: Missing.
Note: Contains a phosphoserine at position 42.
Isoform 4 (identifier: Q15149-4)

Also known as: Plectin-11; 1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSQHQLRVPQ...AVLRASEGKK
Note: Contains a phosphotyrosine at position 26 (By similarity). Contains a phosphoserine at position 21. Contains a phosphoserine at position 20.
Isoform 5 (identifier: Q15149-5)

Also known as: Plectin-8; 1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-174: RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT → MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ
Isoform 6 (identifier: Q15149-6)

Also known as: Plectin-10; 1g;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     134-174: TEEQRVYRRK...RPGPEPAPAT → MSGAGGAFAS...GYLYQQLCCV
Isoform 7 (identifier: Q15149-7)

Also known as: Plectin-7; 1d;

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-174: PAPAT → MKIVP
Isoform 8 (identifier: Q15149-8)

Also known as: Plectin-3; 1e;

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     160-174: QRTLARPGPEPAPAT → MDPSRAIQNEISSLK
Isoform 9 (identifier: Q15149-9)

Also known as: Plectin-2; 1f;

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-174: TPVVPATTQRTLARPGPEPAPAT → MAGPLPDEQDFIQAYEEVREKYK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 46844684Plectin
PRO_0000078135

Regions

Domain175 – 400226Actin-binding
Domain179 – 282104CH 1
Domain295 – 397103CH 2
Repeat645 – 71066Spectrin 1
Repeat740 – 82485Spectrin 2
Repeat837 – 93094Spectrin 3
Repeat1315 – 1415101Spectrin 4
Repeat2826 – 286338Plectin 1
Repeat2864 – 290138Plectin 2
Repeat2902 – 293938Plectin 3
Repeat2940 – 297738Plectin 4
Repeat2981 – 301535Plectin 5
Repeat3116 – 315338Plectin 6
Repeat3154 – 319138Plectin 7
Repeat3192 – 322938Plectin 8
Repeat3230 – 326738Plectin 9
Repeat3268 – 330538Plectin 10
Repeat3306 – 334338Plectin 11
Repeat3485 – 352238Plectin 12
Repeat3523 – 356038Plectin 13
Repeat3561 – 359838Plectin 14
Repeat3599 – 363638Plectin 15
Repeat3640 – 367435Plectin 16
Repeat3820 – 385738Plectin 17
Repeat3858 – 389538Plectin 18
Repeat3896 – 393338Plectin 19
Repeat3934 – 397138Plectin 20
Repeat3975 – 400834Plectin 21
Repeat4063 – 410038Plectin 22
Repeat4101 – 413838Plectin 23
Repeat4139 – 417638Plectin 24
Repeat4177 – 421438Plectin 25
Repeat4218 – 425235Plectin 26
Repeat4265 – 430541Plectin 27
Repeat4319 – 435638Plectin 28
Repeat4408 – 444538Plectin 29
Repeat4446 – 448338Plectin 30
Repeat4484 – 452138Plectin 31
Repeat4522 – 455938Plectin 32
Repeat4560 – 459738Plectin 33
Region1 – 14701470Globular 1
Region1471 – 27551285Central fibrous rod domain
Region2756 – 46841929Globular 2
Region4250 – 430051Binding to intermediate filaments By similarity
Region4625 – 4640164 X 4 AA tandem repeats of G-S-R-X
Coiled coil1469 – 27561288 Potential

Amino acid modifications

Modified residue1131Phosphothreonine Ref.21
Modified residue1251Phosphoserine Ref.7 Ref.12 Ref.21
Modified residue1491Phosphoserine Ref.7 Ref.12 Ref.21
Modified residue7201Phosphoserine Ref.7 Ref.12 Ref.15 Ref.21
Modified residue14351Phosphoserine Ref.7 Ref.11 Ref.21 Ref.24
Modified residue17211Phosphoserine Ref.7
Modified residue17251N6-acetyllysine By similarity
Modified residue17321Phosphoserine Ref.21
Modified residue26361N6-acetyllysine By similarity
Modified residue30331Phosphotyrosine By similarity
Modified residue30531N6-acetyllysine By similarity
Modified residue30911N6-acetyllysine Ref.17
Modified residue33621Phosphotyrosine By similarity
Modified residue34201N6-acetyllysine Ref.17
Modified residue40301Phosphothreonine Ref.7 Ref.15 Ref.21 Ref.24
Modified residue43821Phosphoserine Ref.12 Ref.21
Modified residue43841Phosphoserine By similarity
Modified residue43851Phosphoserine Ref.5 Ref.12
Modified residue43861Phosphoserine Ref.12 Ref.16
Modified residue43891Phosphoserine Ref.12 Ref.16
Modified residue43901Phosphoserine Ref.12
Modified residue43911Phosphoserine Ref.12
Modified residue43921Phosphoserine Ref.12
Modified residue43961Phosphoserine Ref.12 Ref.16 Ref.21
Modified residue44001Phosphoserine Ref.21
Modified residue44111Phosphothreonine Ref.7
Modified residue45391Phosphothreonine; by CDK1 By similarity
Modified residue46131Phosphoserine Ref.12 Ref.16 Ref.21
Modified residue46151Phosphotyrosine By similarity
Modified residue46181Phosphoserine Ref.16
Modified residue46221Phosphoserine Ref.12 Ref.21
Modified residue46261Phosphoserine Ref.12 Ref.15 Ref.16
Modified residue46421Phosphoserine Ref.12 Ref.21

Natural variations

Alternative sequence1 – 174174MVAGM…PAPAT → MSGEDAEVRAVSEDVSNGSS GSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAV IRIA in isoform 2 and isoform 3.
VSP_005030
Alternative sequence1 – 174174MVAGM…PAPAT → MSQHQLRVPQPEGLGRKRTS SEDNLYLAVLRASEGKK in isoform 4.
VSP_023510
Alternative sequence1 – 169169Missing in isoform 7.
VSP_037100
Alternative sequence1 – 159159Missing in isoform 8.
VSP_037101
Alternative sequence1 – 151151Missing in isoform 9.
VSP_037102
Alternative sequence1 – 137137Missing in isoform 5.
VSP_037103
Alternative sequence1 – 133133Missing in isoform 6.
VSP_037104
Alternative sequence134 – 17441TEEQR…PAPAT → MSGAGGAFASPREVLLERPC WLDGGCEPARRGYLYQQLCC V in isoform 6.
VSP_037105
Alternative sequence138 – 17437RVYRR…PAPAT → MEPSGSLFPSLVVVGHVVTL AAVWHWRRGRRWAQDEQ in isoform 5.
VSP_037106
Alternative sequence152 – 17423TPVVP…PAPAT → MAGPLPDEQDFIQAYEEVRE KYK in isoform 9.
VSP_037107
Alternative sequence160 – 17415QRTLA…PAPAT → MDPSRAIQNEISSLK in isoform 8.
VSP_037108
Alternative sequence170 – 1745PAPAT → MKIVP in isoform 7.
VSP_037109
Alternative sequence409 – 4124Missing in isoform 3.
VSP_005031
Natural variant4291L → LL in MD-EBS. Ref.28
VAR_011336
Natural variant6411A → V.
Corresponds to variant rs11136336 [ dbSNP | Ensembl ].
VAR_053585
Natural variant1003 – 10053Missing in MD-EBS.
VAR_011337
Natural variant13211L → V. Ref.2
Corresponds to variant rs3135109 [ dbSNP | Ensembl ].
VAR_060088
Natural variant13861R → Q.
Corresponds to variant rs11136334 [ dbSNP | Ensembl ].
VAR_060089
Natural variant14591H → R.
Corresponds to variant rs55895668 [ dbSNP | Ensembl ].
VAR_062133
Natural variant21101R → W in O-EBS. Ref.29
VAR_015817
Natural variant21501R → W.
Corresponds to variant rs34893635 [ dbSNP | Ensembl ].
VAR_053586
Natural variant21941A → V.
Corresponds to variant rs7002002 [ dbSNP | Ensembl ].
VAR_053587
Natural variant27911S → P.
Corresponds to variant rs7833924 [ dbSNP | Ensembl ].
VAR_053588
Natural variant28211R → W.
Corresponds to variant rs35723243 [ dbSNP | Ensembl ].
VAR_053589
Natural variant29691R → H.
Corresponds to variant rs6558407 [ dbSNP | Ensembl ].
VAR_053590
Natural variant31621V → I.
Corresponds to variant rs35027700 [ dbSNP | Ensembl ].
VAR_053591
Natural variant31711A → V.
Corresponds to variant rs35858667 [ dbSNP | Ensembl ].
VAR_053592
Natural variant34861T → M.
Corresponds to variant rs34725742 [ dbSNP | Ensembl ].
VAR_053593
Natural variant34901G → A.
Corresponds to variant rs35261863 [ dbSNP | Ensembl ].
VAR_053594

Experimental info

Sequence conflict711Y → F in CAA91196. Ref.1
Sequence conflict941P → A in CAA91196. Ref.1
Sequence conflict1391V → L in CAA91196. Ref.1
Sequence conflict1851F → S in CAA91196. Ref.1
Sequence conflict2591N → D in AAB05427. Ref.2
Sequence conflict2591N → D in AAB05428. Ref.2
Sequence conflict5501N → H in CAA91196. Ref.1
Sequence conflict5601V → I in CAA91196. Ref.1
Sequence conflict7061R → Q in CAA91196. Ref.1
Sequence conflict8861Y → N in CAA91196. Ref.1
Sequence conflict10021A → V in CAA91196. Ref.1
Sequence conflict13091V → L in AAB05427. Ref.2
Sequence conflict13091V → L in AAB05428. Ref.2
Sequence conflict13341V → L in AAB05427. Ref.2
Sequence conflict13341V → L in AAB05428. Ref.2
Sequence conflict15341M → I in CAA91196. Ref.1
Sequence conflict16621A → T in AAB05427. Ref.2
Sequence conflict16621A → T in AAB05428. Ref.2
Sequence conflict1688 – 16903RLR → WLC in CAA91196. Ref.1
Sequence conflict17671E → Q in CAA91196. Ref.1
Sequence conflict17891A → L in CAA91196. Ref.1
Sequence conflict19101R → K in CAA91196. Ref.1
Sequence conflict21541K → N in AAB05427. Ref.2
Sequence conflict21541K → N in AAB05428. Ref.2
Sequence conflict21541K → N in CAA65765. Ref.2
Sequence conflict21541K → N in AAR95680. Ref.3
Sequence conflict21541K → N in AAR95682. Ref.3
Sequence conflict21541K → N in AAR95683. Ref.3
Sequence conflict21601R → S in CAA91196. Ref.1
Sequence conflict22151Q → R in CAA91196. Ref.1
Sequence conflict22441S → A in CAA91196. Ref.1
Sequence conflict22441S → A in AAB05427. Ref.2
Sequence conflict22441S → A in AAB05428. Ref.2
Sequence conflict22441S → A in CAA65765. Ref.2
Sequence conflict30271K → E in AAB05427. Ref.2
Sequence conflict30271K → E in AAB05428. Ref.2
Sequence conflict33101A → E in CAA91196. Ref.1
Sequence conflict33611L → F in CAA91196. Ref.1
Sequence conflict34081L → F in CAA91196. Ref.1
Sequence conflict34471A → S in CAA91196. Ref.1
Sequence conflict35311A → G in CAA91196. Ref.1
Sequence conflict35801S → R in CAA91196. Ref.1
Sequence conflict35891Q → K in CAA91196. Ref.1
Sequence conflict35961Q → E in CAA91196. Ref.1
Sequence conflict36161H → N in CAA91196. Ref.1
Sequence conflict36861A → V in CAA91196. Ref.1
Sequence conflict37861A → G in CAA91196. Ref.1
Sequence conflict38081R → K in CAA91196. Ref.1
Sequence conflict38161A → G in CAA91196. Ref.1
Sequence conflict38211C → F in CAA91196. Ref.1
Sequence conflict39151Q → K in CAA91196. Ref.1
Sequence conflict39991R → K in CAA91196. Ref.1
Sequence conflict40071T → S in CAA91196. Ref.1
Sequence conflict44671F → L in CAA91196. Ref.1

Secondary structure

.............................................................................. 4684
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Plectin-6) [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: 04772E4F70A304C8

FASTA4,684531,791
        10         20         30         40         50         60 
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLRARGL 

        70         80         90        100        110        120 
VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRTPHVQAVQ 

       130        140        150        160        170        180 
GPLGSPPKRG PLPTEEQRVY RRKELEEVSP ETPVVPATTQ RTLARPGPEP APATDERDRV 

       190        200        210        220        230        240 
QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV 

       250        260        270        280        290        300 
QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 

       310        320        330        340        350        360 
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ TNLENLDQAF 

       370        380        390        400        410        420 
SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR ANELQLRWQE 

       430        440        450        460        470        480 
YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE ADKNRSKGIY 

       490        500        510        520        530        540 
QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM 

       550        560        570        580        590        600 
EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 

       610        620        630        640        650        660 
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR RPELEDSTLR 

       670        680        690        700        710        720 
YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE RARSDEGQLS 

       730        740        750        760        770        780 
PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN EKEEEEVGFD 

       790        800        810        820        830        840 
WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ 

       850        860        870        880        890        900 
WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 

       910        920        930        940        950        960 
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC DYKQVEVTVH 

       970        980        990       1000       1010       1020 
KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE AQHQALVTLW 

      1030       1040       1050       1060       1070       1080 
HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY QAFLRDSQDA 

      1090       1100       1110       1120       1130       1140 
GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT 

      1150       1160       1170       1180       1190       1200 
VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 

      1210       1220       1230       1240       1250       1260 
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK EAQAVPATLP 

      1270       1280       1290       1300       1310       1320 
ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE VERWRERVAQ 

      1330       1340       1350       1360       1370       1380 
LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI QAMPLADSQA 

      1390       1400       1410       1420       1430       1440 
VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP 

      1450       1460       1470       1480       1490       1500 
KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 

      1510       1520       1530       1540       1550       1560 
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ QKRSIQEELQ 

      1570       1580       1590       1600       1610       1620 
QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG ELQALRARAE 

      1630       1640       1650       1660       1670       1680 
EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR ALQALEELRL 

      1690       1700       1710       1720       1730       1740 
QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV 

      1750       1760       1770       1780       1790       1800 
AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 

      1810       1820       1830       1840       1850       1860 
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ ELIRLRAETE 

      1870       1880       1890       1900       1910       1920 
QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR AEEESRSTSE 

      1930       1940       1950       1960       1970       1980 
KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER VLAEKLAAIG 

      1990       2000       2010       2020       2030       2040 
EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD 

      2050       2060       2070       2080       2090       2100 
SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 

      2110       2120       2130       2140       2150       2160 
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER LKAKVEEARR 

      2170       2180       2190       2200       2210       2220 
LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ SVLDQLRGEA 

      2230       2240       2250       2260       2270       2280 
EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA AAEKLRKEAE 

      2290       2300       2310       2320       2330       2340 
QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN 

      2350       2360       2370       2380       2390       2400 
LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 

      2410       2420       2430       2440       2450       2460 
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK EKMQAVQEAT 

      2470       2480       2490       2500       2510       2520 
RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ RQLEMSAEAE 

      2530       2540       2550       2560       2570       2580 
RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT LEIQRQQSDH 

      2590       2600       2610       2620       2630       2640 
DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL 

      2650       2660       2670       2680       2690       2700 
QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 

      2710       2720       2730       2740       2750       2760 
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE EVTASQVAAT 

      2770       2780       2790       2800       2810       2820 
KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA QGHTTVDELA 

      2830       2840       2850       2860       2870       2880 
RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ AASGFLLDPV 

      2890       2900       2910       2920       2930       2940 
RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI 

      2950       2960       2970       2980       2990       3000 
RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 

      3010       3020       3030       3040       3050       3060 
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP FGKFQGKTVT 

      3070       3080       3090       3100       3110       3120 
IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC FEGLRSLVPA 

      3130       3140       3150       3160       3170       3180 
AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE AGQKLSIYNA 

      3190       3200       3210       3220       3230       3240 
LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT 

      3250       3260       3270       3280       3290       3300 
GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 

      3310       3320       3330       3340       3350       3360 
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS EKAARARQEE 

      3370       3380       3390       3400       3410       3420 
LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ FRTGKVTVEK 

      3430       3440       3450       3460       3470       3480 
VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD GKTTVKDLSE 

      3490       3500       3510       3520       3530       3540 
LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR 

      3550       3560       3570       3580       3590       3600 
NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 

      3610       3620       3630       3640       3650       3660 
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF DPNTHENLTY 

      3670       3680       3690       3700       3710       3720 
RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID IPGGGSHGGS 

      3730       3740       3750       3760       3770       3780 
TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR QQGLASYDYV 

      3790       3800       3810       3820       3830       3840 
RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT 

      3850       3860       3870       3880       3890       3900 
LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 

      3910       3920       3930       3940       3950       3960 
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR LGFHLPLEVA 

      3970       3980       3990       4000       4010       4020 
YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL LLPLSDARKL 

      4030       4040       4050       4060       4070       4080 
TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT 

      4090       4100       4110       4120       4130       4140 
KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK 

      4150       4160       4170       4180       4190       4200 
LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 

      4210       4220       4230       4240       4250       4260 
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ TGLCLLPLKE 

      4270       4280       4290       4300       4310       4320 
KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE QECEWEEITI 

      4330       4340       4350       4360       4370       4380 
SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA DMLSGNAGGF 

      4390       4400       4410       4420       4430       4440 
RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV 

      4450       4460       4470       4480       4490       4500 
DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 

      4510       4520       4530       4540       4550       4560 
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ RGTVDARTAQ 

      4570       4580       4590       4600       4610       4620 
KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG YYSPYSVSGS 

      4630       4640       4650       4660       4670       4680 
GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS GSSASLGGPE 


SAVA 

« Hide

Isoform 2 (Plectin-1) (1c) [UniParc].

Checksum: 7EAEA5A83DEF52EA
Show »

FASTA4,574518,473
Isoform 3 [UniParc].

Checksum: A0AF260B8C095C8D
Show »

FASTA4,570518,032
Isoform 4 (Plectin-11) (1a) [UniParc].

Checksum: 0A1A2AB2E557110A
Show »

FASTA4,547516,198
Isoform 5 (Plectin-8) (1b) [UniParc].

Checksum: 0EC98F109B723779
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FASTA4,547516,276
Isoform 6 (Plectin-10) (1g) [UniParc].

Checksum: C2E0FDA51BC17BF2
Show »

FASTA4,551516,479
Isoform 7 (Plectin-7) (1d) [UniParc].

Checksum: C8701AD6D1C1B26E
Show »

FASTA4,515512,604
Isoform 8 (Plectin-3) (1e) [UniParc].

Checksum: 37A4DFAB46C3B4DD
Show »

FASTA4,525513,706
Isoform 9 (Plectin-2) (1f) [UniParc].

Checksum: 5D6382389A66B955
Show »

FASTA4,533514,775

References

« Hide 'large scale' references
[1]"Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)."
Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.
Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[2]"Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization."
McLean W.H.I., Pulkkinen L., Smith F.J.D., Rugg E.L., Lane E.B., Bullrich F., Burgeson R.E., Amano S., Hudson D.L., Owaribe K., McGrath J.A., McMillan J.R., Eady R.A.J., Leigh I.M., Christiano A.M., Uitto J.
Genes Dev. 10:1724-1735(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, VARIANT VAL-1321.
[3]"Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
Zhang T., Haws P., Wu Q.
Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 14-21; 209-227; 237-248; 301-316; 329-336; 350-365; 372-417; 510-517; 588-597; 631-675; 697-706; 714-724; 734-740; 751-764; 857-869; 897-908; 927-934; 1029-1037; 1045-1052; 1076-1088; 1131-1139; 1166-1175; 1187-1210; 1216-1224; 1227-1243; 1251-1266; 1274-1291; 1318-1335; 1338-1344; 1351-1364; 1366-1382; 1411-1438; 1473-1479; 1499-1508; 1554-1563; 1596-1603; 1606-1616; 1628-1638; 1649-1657; 1671-1679; 1699-1709; 1732-1744; 1783-1792; 1825-1833; 1846-1854; 1867-1875; 1888-1908; 1976-1994; 2006-2014; 2048-2055; 2058-2068; 2079-2087; 2098-2108; 2130-2139; 2142-2150; 2172-2182; 2199-2217; 2310-2316; 2319-2329; 2340-2348; 2361-2379; 2402-2409; 2420-2429; 2432-2442; 2462-2473; 2483-2503; 2512-2521; 2565-2575; 2587-2594; 2651-2663; 2685-2693; 2705-2761; 2768-2787; 2795-2821; 2833-2841; 2847-2881; 2885-2903; 2942-2968; 2979-3007; 3028-3039; 3045-3053; 3095-3106; 3109-3127; 3132-3139; 3146-3154; 3175-3183; 3213-3231; 3244-3259; 3270-3285; 3289-3297; 3317-3335; 3356-3368; 3374-3384; 3424-3436; 3447-3469; 3477-3485; 3506-3513; 3519-3540; 3544-3568; 3601-3637; 3648-3661; 3667-3676; 3686-3702; 3739-3749; 3771-3781; 3784-3804; 3839-3878; 3887-3897; 3926-3963; 3969-3999; 4004-4018; 4027-4060; 4084-4091; 4122-4138; 4159-4167; 4179-4205; 4278-4296; 4339-4348; 4354-4360; 4384-4401; 4429-4447; 4467-4475; 4492-4500; 4543-4551; 4590-4627 AND 4668-4684, PHOSPHORYLATION AT SER-4385, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[6]"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH COL17A1, SUBCELLULAR LOCATION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-4030 AND THR-4411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-4382; SER-4385; SER-4386; SER-4389; SER-4390; SER-4391; SER-4392; SER-4396; SER-4613; SER-4622; SER-4626 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOR1A.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; THR-4030 AND SER-4626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396; SER-4613; SER-4618 AND SER-4626, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3091 AND LYS-3420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy."
Gundesli H., Talim B., Korkusuz P., Balci-Hayta B., Cirak S., Akarsu N.A., Topaloglu H., Dincer P.
Am. J. Hum. Genet. 87:834-841(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ISOFORM 9, INVOLVEMENT IN LGMD2Q.
[19]"BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DST.
[20]"Plectin deficiency leads to both muscular dystrophy and pyloric atresia in epidermolysis bullosa simplex."
Natsuga K., Nishie W., Shinkuma S., Arita K., Nakamura H., Ohyama M., Osaka H., Kambara T., Hirako Y., Shimizu H.
Hum. Mutat. 31:E1687-E1698(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MD-EBS AND EBS-PA.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4396; SER-4400; SER-4613; SER-4622 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
Maiweilidan Y., Klauza I., Kordeli E.
Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANK3.
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 AND THR-4030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain."
Sonnenberg A., Rojas A.M., de Pereda J.M.
J. Mol. Biol. 368:1379-1391(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
[26]"Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4."
Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.
Structure 11:615-625(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
[27]"Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy."
Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.
Hum. Mol. Genet. 5:1539-1546(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
[28]"A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency."
Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.
Am. J. Pathol. 158:617-625(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MD-EBS LEU-429 INS.
[29]"A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations."
Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.
J. Invest. Dermatol. 118:87-93(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT O-EBS TRP-2110.
[30]"Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin."
Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.
J. Invest. Dermatol. 121:1344-1348(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EBS-PA.
+Additional computationally mapped references.

Web resources

Wikipedia

Plectin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z54367 Genomic DNA. Translation: CAA91196.1.
U53204 mRNA. Translation: AAB05427.1.
U63610, U63609 Genomic DNA. Translation: AAB05428.1.
X97053 mRNA. Translation: CAA65765.1.
AY480044 mRNA. Translation: AAR95677.1.
AY480045 mRNA. Translation: AAR95678.1.
AY480046 mRNA. Translation: AAR95679.1.
AY480047 mRNA. Translation: AAR95680.1.
AY480048 mRNA. Translation: AAR95681.1.
AY480049 mRNA. Translation: AAR95682.1.
AY480050 mRNA. Translation: AAR95683.1.
AY480051 mRNA. Translation: AAR95684.1.
AC109322 Genomic DNA. No translation available.
CCDSCCDS43769.1. [Q15149-2]
CCDS43770.1. [Q15149-9]
CCDS43771.1. [Q15149-8]
CCDS43772.1. [Q15149-1]
CCDS43773.1. [Q15149-5]
CCDS43774.1. [Q15149-6]
CCDS43775.1. [Q15149-4]
CCDS47936.1. [Q15149-7]
PIRA59404. C59404.
G02520.
RefSeqNP_000436.2. NM_000445.4. [Q15149-2]
NP_958780.1. NM_201378.3. [Q15149-9]
NP_958781.1. NM_201379.2. [Q15149-8]
NP_958782.1. NM_201380.3. [Q15149-1]
NP_958783.1. NM_201381.2. [Q15149-7]
NP_958784.1. NM_201382.3. [Q15149-5]
NP_958785.1. NM_201383.2. [Q15149-6]
NP_958786.1. NM_201384.2. [Q15149-4]
UniGeneHs.434248.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MB8X-ray2.15A175-403[»]
2ODUX-ray2.30A410-640[»]
2ODVX-ray2.05A410-640[»]
3F7PX-ray2.75A/B175-403[»]
3PDYX-ray2.22A/B653-858[»]
3PE0X-ray2.95A/B750-1028[»]
4GDOX-ray1.70A/B/C/D/E/F1492-1530[»]
ProteinModelPortalQ15149.
SMRQ15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111355. 54 interactions.
IntActQ15149. 25 interactions.
MINTMINT-257064.

Chemistry

BindingDBQ15149.
ChEMBLCHEMBL1293240.

PTM databases

PhosphoSiteQ15149.

Polymorphism databases

DMDM209572726.

Proteomic databases

MaxQBQ15149.
PaxDbQ15149.
PRIDEQ15149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322810; ENSP00000323856; ENSG00000178209. [Q15149-1]
ENST00000345136; ENSP00000344848; ENSG00000178209. [Q15149-4]
ENST00000354589; ENSP00000346602; ENSG00000178209. [Q15149-5]
ENST00000354958; ENSP00000347044; ENSG00000178209. [Q15149-8]
ENST00000356346; ENSP00000348702; ENSG00000178209. [Q15149-9]
ENST00000357649; ENSP00000350277; ENSG00000178209. [Q15149-6]
ENST00000398774; ENSP00000381756; ENSG00000178209. [Q15149-7]
ENST00000436759; ENSP00000388180; ENSG00000178209. [Q15149-2]
ENST00000527096; ENSP00000434583; ENSG00000178209. [Q15149-3]
ENST00000561589; ENSP00000454242; ENSG00000261109. [Q15149-7]
ENST00000561919; ENSP00000455773; ENSG00000261109. [Q15149-8]
ENST00000564962; ENSP00000456105; ENSG00000261109. [Q15149-4]
ENST00000565080; ENSP00000454566; ENSG00000261109. [Q15149-5]
ENST00000565268; ENSP00000455881; ENSG00000261109. [Q15149-2]
ENST00000565557; ENSP00000457504; ENSG00000261109. [Q15149-6]
ENST00000567302; ENSP00000456732; ENSG00000261109. [Q15149-9]
ENST00000568193; ENSP00000455828; ENSG00000261109. [Q15149-1]
ENST00000568204; ENSP00000454559; ENSG00000261109. [Q15149-3]
GeneID5339.
KEGGhsa:5339.
UCSCuc003zab.1. human. [Q15149-4]
uc003zac.1. human. [Q15149-6]
uc003zad.2. human. [Q15149-5]
uc003zae.1. human. [Q15149-7]
uc003zaf.1. human. [Q15149-1]
uc003zag.1. human. [Q15149-8]
uc003zah.2. human. [Q15149-9]
uc003zaj.2. human. [Q15149-2]

Organism-specific databases

CTD5339.
GeneCardsGC08M144989.
GeneReviewsPLEC.
H-InvDBHIX0168901.
HGNCHGNC:9069. PLEC.
HPACAB003847.
HPA025967.
HPA029906.
MIM131950. phenotype.
226670. phenotype.
601282. gene.
612138. phenotype.
613723. phenotype.
neXtProtNX_Q15149.
Orphanet254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
257. Epidermolysis bullosa simplex with muscular dystrophy.
158684. Epidermolysis bullosa simplex with pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
PharmGKBPA33399.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOVERGENHBG053616.
InParanoidQ15149.
KOK10388.
OMAYLNKDTH.
PhylomeDBQ15149.
TreeFamTF335163.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ15149.
BgeeQ15149.
CleanExHS_PLEC1.
GenevestigatorQ15149.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLEC. human.
EvolutionaryTraceQ15149.
GeneWikiPlectin.
GenomeRNAi5339.
NextBio20680.
PROQ15149.
SOURCESearch...

Entry information

Entry namePLEC_HUMAN
AccessionPrimary (citable) accession number: Q15149
Secondary accession number(s): Q15148 expand/collapse secondary AC list , Q16640, Q6S376, Q6S377, Q6S378, Q6S379, Q6S380, Q6S381, Q6S382, Q6S383
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM